Rapid protein purification is an important requirement in many bioengineering applications where significant amounts of time are currently spent purifying proteins from heterogeneous samples. There are currently a number of approaches for performing bioseparation, but these approaches are expensive, time consuming, can require specialized treatments.
A variety of approaches currently exist for purifying recombinant proteins such as using a poly-histidine tag, glutathione S-transferase (GST) fusions or fusion to an elastin-like peptide (ELP). In the case of ELPs, a fusion protein can be precipitated from solution by increasing the temperature of the sample (Banki, et al., Nat Meth, vol. 2, no. 9, pp. 659-662, 2005; Fong et al, Trends in Biotechnology, vol. 28, no. 5, pp. 272-279, May 2010). One limitation of ELP technology is that increased temperature can adversely affect the stability of fusion proteins. Another limitation of ELP technology is that inducing temperature changes are difficult in large scale preparations.
There is a need for improved purification methods for rapid purification of molecules (e.g. exogenously expressed proteins) from heterogeneous samples in a rapid manner and with high levels of recovery. This invention addresses these needs.